人肝细胞膜上嘌呤受体的特性研究
Characterization of purinoceptors present on human liver plasma membranes.
作者信息
Keppens S, Vandekerckhove A, De Wulf H
机构信息
Afdeling Biochemie, Katholieke Universiteit Leuven, Belgium.
出版信息
FEBS Lett. 1989 May 8;248(1-2):137-40. doi: 10.1016/0014-5793(89)80448-x.
Using ATP alpha 35S as radioligand, we have detected the presence of specific purinoceptors on human liver plasma membranes. They are characterized by a Kd value of 0.19 microM and a Bmax of 24 pmol/mg membrane protein. These purinoceptors belong to the P2Y subclass as demonstrated by the high degree of similarity with rat liver purinoceptors, previously shown to be P2Y [(1986) Biochem. J. 240, 367-371] and known to be involved in the control of liver glycogenolysis.
以ATPα35S作为放射性配体，我们检测到了人肝细胞膜上存在特异性嘌呤受体。它们的特征是解离常数（Kd）值为0.19微摩尔，最大结合容量（Bmax）为24皮摩尔/毫克膜蛋白。这些嘌呤受体属于P2Y亚类，这是通过与大鼠肝嘌呤受体的高度相似性证明的，先前已表明大鼠肝嘌呤受体为P2Y [（1986年）《生物化学杂志》240, 367 - 371]，并且已知其参与肝脏糖原分解的调控。
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